Kinetic parameters of wild-type and one-point mutants.

NIAID Data Ecosystem2026-03-07 收录

酶动力学参数

蛋白突变效应

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*The data was referenced from our previous work [11].

创建时间：

2013-03-15

Documentation of an Imperative To Improve Methods for Predicting Membrane Protein Stability

膜蛋白稳定性

蛋白突变效应

There is a compelling and growing need to accurately predict the impact of amino acid mutations on protein stability for problems in personalized medicine and other applications. Here the ability of 1

NIAID Data Ecosystem110

Kinetics parameters of wild-type GOOX and CBM fusions on cellotetraose.

酶动力学参数

纤维四糖底物催化

Errors indicate standard deviations; n = 3. a Standard deviations (SD) for kcat/Km values were calculated using following formula: SD kcat/Km = kcat/Km × [SQRT((SD(Km)/Km)2 + (SD(kcat)/kcat)2)]. Aster

NIAID Data Ecosystem30

Summary of kinetic constants for hydrolysis of cocaine, acetylcholine (ACh), and butyrylthiocholine (BThCh) by wild type mouse BChE as previously determined [14], [15] and mCocH, determined as described in Methods.

酶动力学参数

可卡因代谢

Given constants are mean values of three or more experiments. Standard error of determination was typically 30% or less of the constant value.

NIAID Data Ecosystem20

Kinetic parameters (± SD) of recombinant enzymes with physiological substrates at physiological pH.

酶动力学参数

重组酶催化

1kcat values were determined from the rate of Pi formation. 2As the detection of two Pi corresponds to one cleavage event, the actual rate is only half of the calculated number of Pi molecules release

NIAID Data Ecosystem110

Yeast Hsp82 N-terminal domain: effects of mutants 98-99 KS-AA

蛋白突变效应

分子伴侣结构

Yeast Hsp82 N-terminal domain: effects of mutants 98-99 KS-AA Descriptor: ATP-dependent molecular chaperone HSP82 Authors: Immormino, R.M, Gewirth, D.T. Deposit date: 2008-01-19 Release date: 2008-07-

Protein Data Bank Japan2023-08-30 更新20

Kinetic parameters of wild-type and one-point mutants.

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